Open AccessCrystallization and preliminary X‐ray study of alkaline β‐mannanase from the alkaliphilic Bacillus sp. N16‐5
Author(s) -
Zhao Yueju,
Zhang Yunhua,
Gao Feng,
Xue Yanfen,
Zeng Yan,
Ma Yanhe
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108028571
Subject(s) - orthorhombic crystal system , crystallization , recombinant dna , molecular replacement , bacillus (shape) , crystallography , enzyme , chemistry , resolution (logic) , crystal structure , biology , microbiology and biotechnology , biochemistry , organic chemistry , gene , artificial intelligence , computer science
The catalytic domain of an alkaline β‐mannanase from the alkaliphilic Bacillus sp. N16‐5 has been expressed and purified. The recombinant enzyme was crystallized using the hanging‐drop vapour‐diffusion method at 298 K. X‐ray diffraction data were collected to 1.6 Å resolution. The crystal belonged to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 59.03, b = 63.31, c = 83.34 Å. Initial phasing was carried out by molecular replacement using the three‐dimensional structure of a mannanase from the alkaliphilic Bacillus sp. JAMB602 as a search model.